ReviewInternational journal of molecular sciences2018
The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results.
Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- pH-Dependent Stability and Cooperativity of Protein Unfolding from Differential Scanning Calorimetry Using FitFoldData.Biomolecules · 2026Article
- Hydrophobic Ion Pairing Improves Protein Thermal Stability and Lipid Nanocarrier Integration through Controlled Surface Modification.ACS nanoscience Au · 2026Article
- Evolutionary algorithm-optimized feature fusion for accurate classification of shredded tobacco using multi-sensor data.Frontiers in plant science · 2025Article
- Regium-π Bonds Involving Nucleobases: Theoretical Study and Biological Implications.Inorganic chemistry · 2023Article
- Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated with Rare Severe Distal Neuropathies.International journal of molecular sciences · 2023Article
- Dihydrogen Bonding-Seen through the Eyes of Vibrational Spectroscopy.Molecules (Basel, Switzerland) · 2022Article
- Ionic Liquid-Based Strategy for Predicting Protein Aggregation Propensity and Thermodynamic Stability.JACS Au · 2022Article
- Combining a Genetically Engineered Oxidase with Hydrogen-Bonded Organic Frameworks (HOFs) for Highly Efficient Biocomposites.Angewandte Chemie (International ed. in English) · 2022Article
- Zinc Binding to NAP-Type Neuroprotective Peptides: Nuclear Magnetic Resonance Studies and Molecular Modeling.Pharmaceuticals (Basel, Switzerland) · 2021Article
- From Critical Point to Critical Point: The Two-States Model Describes Liquid Water Self-Diffusion from 623 to 126 K.Molecules (Basel, Switzerland) · 2021Article
- Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies.Communications biology · 2021Article
- Article
- Comparative modelling studies of fruit bromelain using molecular dynamics simulation.Journal of molecular modeling · 2020Article
- Article
- The Proton Density of States in Confined Water (HInternational journal of molecular sciences · 2019Article
- Aggregation States of AInternational journal of molecular sciences · 2019Article
- Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The biological activity of proteins depends on their three-dimensional structure, known as the native state. The main force driving the correct folding mechanism is the hydrophobic effect and when this folding kinetics is altered, aggregation phenomena intervene causing the occurrence of illnesses such as Alzheimer and Parkinson's diseases. The other important effect is performed by water molecules and by their ability to form a complex network of hydrogen bonds whose dynamics influence the mobility of protein amino acids. In this work, we review the recent results obtained by means of spectroscopic techniques, such as Fourier Transform Infrared (FTIR) and Nuclear Magnetic Resonance (NMR) spectroscopies, on hydrated lysozyme. In particular, we explore the Energy Landscape from the thermal region of configurational stability up to that of the irreversible denaturation. The importance of the coupling between the solute and the solvent will be highlighted as well as the different behaviors of hydrophilic and hydrophobic moieties of protein amino acid residues.
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